1xw3: Difference between revisions

Revision as of 16:59, 21 February 2008

Crystal Structure of Human Sulfiredoxin (Srx)

OverviewOverview

Sufiredoxins (Srx) repair the inactivated forms of typical two-Cys peroxiredoxins (Prx) implicated in hydrogen peroxide-mediated cell signaling. The reduction of the cysteine sulfinic acid moiety within the active site of the Prx by Srx involves novel sulfur chemistry and the use of ATP and Mg(2+). The 1.65 A crystal structure of human Srx (hSrx) exhibits a new protein fold and a unique nucleotide binding motif containing the Gly98-Cys99-His100-Arg101 sequence at the N-terminus of an alpha-helix. HPLC analysis of the reaction products has confirmed that the site of ATP cleavage is between the beta- and gamma-phosphate groups. Cys99 and the gamma-phosphate of ATP, modeled within the active site of the 2.0 A ADP product complex structure, are adjacent to large surface depressions containing additional conserved residues. These features and the necessity for significant remodeling of the Prx structure suggest that the interactions between hSrx and typical two-Cys Prxs are specific. Moreover, the concave shape of the hSrx active site surface appears to be ideally suited to interacting with the convex surface of the toroidal Prx decamer.

About this StructureAbout this Structure

1XW3 is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for the retroreduction of inactivated peroxiredoxins by human sulfiredoxin., Jonsson TJ, Murray MS, Johnson LC, Poole LB, Lowther WT, Biochemistry. 2005 Jun 21;44(24):8634-42. PMID:15952770

Page seeded by OCA on Thu Feb 21 15:59:13 2008

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OCA

@@ Line 1: / Line 1: @@
-[[Image:1xw3.gif|left|200px]]<br />
+[[Image:1xw3.gif|left|200px]]<br /><applet load="1xw3" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1xw3" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1xw3, resolution 1.65&Aring;" />
 '''Crystal Structure of Human Sulfiredoxin (Srx)'''<br />
 ==Overview==
-Sufiredoxins (Srx) repair the inactivated forms of typical two-Cys, peroxiredoxins (Prx) implicated in hydrogen peroxide-mediated cell, signaling. The reduction of the cysteine sulfinic acid moiety within the, active site of the Prx by Srx involves novel sulfur chemistry and the use, of ATP and Mg(2+). The 1.65 A crystal structure of human Srx (hSrx), exhibits a new protein fold and a unique nucleotide binding motif, containing the Gly98-Cys99-His100-Arg101 sequence at the N-terminus of an, alpha-helix. HPLC analysis of the reaction products has confirmed that the, site of ATP cleavage is between the beta- and gamma-phosphate groups., Cys99 and the gamma-phosphate of ATP, modeled within the active site of, the 2.0 A ADP product complex structure, are adjacent to large surface, depressions containing additional conserved residues. These features and, the necessity for significant remodeling of the Prx structure suggest that, the interactions between hSrx and typical two-Cys Prxs are specific., Moreover, the concave shape of the hSrx active site surface appears to be, ideally suited to interacting with the convex surface of the toroidal Prx, decamer.
+Sufiredoxins (Srx) repair the inactivated forms of typical two-Cys peroxiredoxins (Prx) implicated in hydrogen peroxide-mediated cell signaling. The reduction of the cysteine sulfinic acid moiety within the active site of the Prx by Srx involves novel sulfur chemistry and the use of ATP and Mg(2+). The 1.65 A crystal structure of human Srx (hSrx) exhibits a new protein fold and a unique nucleotide binding motif containing the Gly98-Cys99-His100-Arg101 sequence at the N-terminus of an alpha-helix. HPLC analysis of the reaction products has confirmed that the site of ATP cleavage is between the beta- and gamma-phosphate groups. Cys99 and the gamma-phosphate of ATP, modeled within the active site of the 2.0 A ADP product complex structure, are adjacent to large surface depressions containing additional conserved residues. These features and the necessity for significant remodeling of the Prx structure suggest that the interactions between hSrx and typical two-Cys Prxs are specific. Moreover, the concave shape of the hSrx active site surface appears to be ideally suited to interacting with the convex surface of the toroidal Prx decamer.
 ==About this Structure==
-XW3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with PO4 and MPD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XW3 OCA].
+XW3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XW3 OCA].
 ==Reference==
@@ Line 14: / Line 13: @@
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Johnson, L.C.]]
+[[Category: Johnson, L C.]]
-[[Category: Jonsson, T.J.]]
+[[Category: Jonsson, T J.]]
-[[Category: Lowther, W.T.]]
+[[Category: Lowther, W T.]]
-[[Category: Murray, M.S.]]
+[[Category: Murray, M S.]]
-[[Category: Poole, L.B.]]
+[[Category: Poole, L B.]]
 [[Category: MPD]]
 [[Category: PO4]]
@@ Line 26: / Line 25: @@
 [[Category: sulfinic acid]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:11:30 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:59:13 2008''